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Database: UniProt
Entry: A0A364K7F2_9BACL
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ID   A0A364K7F2_9BACL        Unreviewed;       732 AA.
AC   A0A364K7F2;
DT   07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT   07-NOV-2018, sequence version 1.
DT   24-JAN-2024, entry version 19.
DE   RecName: Full=DNA topoisomerase 3 {ECO:0000256|HAMAP-Rule:MF_00953};
DE            EC=5.6.2.1 {ECO:0000256|HAMAP-Rule:MF_00953};
DE   AltName: Full=DNA topoisomerase III {ECO:0000256|HAMAP-Rule:MF_00953};
GN   Name=topB {ECO:0000256|HAMAP-Rule:MF_00953};
GN   ORFNames=DL897_04300 {ECO:0000313|EMBL:RAL26226.1};
OS   Thermoflavimicrobium daqui.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Thermoactinomycetaceae;
OC   Thermoflavimicrobium.
OX   NCBI_TaxID=2137476 {ECO:0000313|EMBL:RAL26226.1, ECO:0000313|Proteomes:UP000251213};
RN   [1] {ECO:0000313|EMBL:RAL26226.1, ECO:0000313|Proteomes:UP000251213}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=FBKL4.011 {ECO:0000313|EMBL:RAL26226.1,
RC   ECO:0000313|Proteomes:UP000251213};
RA   Wang X., Zhou H.;
RT   "Thermoflavimicrobium daqus sp. nov., a thermophilic microbe isolated from
RT   Moutai-flavour Daqu.";
RL   Submitted (JUN-2018) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:RAL26226.1, ECO:0000313|Proteomes:UP000251213}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=FBKL4.011 {ECO:0000313|EMBL:RAL26226.1,
RC   ECO:0000313|Proteomes:UP000251213};
RA   Zhirakovskaya E.;
RL   Submitted (JUN-2018) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Releases the supercoiling and torsional tension of DNA, which
CC       is introduced during the DNA replication and transcription, by
CC       transiently cleaving and rejoining one strand of the DNA duplex.
CC       Introduces a single-strand break via transesterification at a target
CC       site in duplex DNA. The scissile phosphodiester is attacked by the
CC       catalytic tyrosine of the enzyme, resulting in the formation of a DNA-
CC       (5'-phosphotyrosyl)-enzyme intermediate and the expulsion of a 3'-OH
CC       DNA strand. The free DNA strand then undergoes passage around the
CC       unbroken strand, thus removing DNA supercoils. Finally, in the
CC       religation step, the DNA 3'-OH attacks the covalent intermediate to
CC       expel the active-site tyrosine and restore the DNA phosphodiester
CC       backbone. {ECO:0000256|HAMAP-Rule:MF_00953}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP-independent breakage of single-stranded DNA, followed by
CC         passage and rejoining.; EC=5.6.2.1;
CC         Evidence={ECO:0000256|ARBA:ARBA00000213, ECO:0000256|HAMAP-
CC         Rule:MF_00953};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_00953};
CC   -!- SIMILARITY: Belongs to the type IA topoisomerase family.
CC       {ECO:0000256|ARBA:ARBA00009446, ECO:0000256|HAMAP-Rule:MF_00953}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {ECO:0000256|HAMAP-Rule:MF_00953}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:RAL26226.1}.
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DR   EMBL; QJKK01000002; RAL26226.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A364K7F2; -.
DR   OrthoDB; 9803554at2; -.
DR   Proteomes; UP000251213; Unassembled WGS sequence.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0003917; F:DNA topoisomerase type I (single strand cut, ATP-independent) activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0006265; P:DNA topological change; IEA:UniProtKB-UniRule.
DR   CDD; cd00186; TOP1Ac; 1.
DR   CDD; cd03362; TOPRIM_TopoIA_TopoIII; 1.
DR   Gene3D; 3.40.50.140; -; 1.
DR   Gene3D; 1.10.460.10; Topoisomerase I, domain 2; 1.
DR   Gene3D; 2.70.20.10; Topoisomerase I, domain 3; 1.
DR   Gene3D; 1.10.290.10; Topoisomerase I, domain 4; 1.
DR   HAMAP; MF_00953; Topoisom_3_prok; 1.
DR   InterPro; IPR000380; Topo_IA.
DR   InterPro; IPR003601; Topo_IA_2.
DR   InterPro; IPR023406; Topo_IA_AS.
DR   InterPro; IPR013497; Topo_IA_cen.
DR   InterPro; IPR013824; Topo_IA_cen_sub1.
DR   InterPro; IPR013825; Topo_IA_cen_sub2.
DR   InterPro; IPR013826; Topo_IA_cen_sub3.
DR   InterPro; IPR023405; Topo_IA_core_domain.
DR   InterPro; IPR003602; Topo_IA_DNA-bd_dom.
DR   InterPro; IPR005738; TopoIII.
DR   InterPro; IPR006171; TOPRIM_domain.
DR   InterPro; IPR034144; TOPRIM_TopoIII.
DR   NCBIfam; TIGR01056; topB; 1.
DR   PANTHER; PTHR11390:SF21; DNA TOPOISOMERASE 3-ALPHA; 1.
DR   PANTHER; PTHR11390; PROKARYOTIC DNA TOPOISOMERASE; 1.
DR   Pfam; PF01131; Topoisom_bac; 1.
DR   Pfam; PF01751; Toprim; 1.
DR   PRINTS; PR00417; PRTPISMRASEI.
DR   SMART; SM00437; TOP1Ac; 1.
DR   SMART; SM00436; TOP1Bc; 1.
DR   SMART; SM00493; TOPRIM; 1.
DR   SUPFAM; SSF56712; Prokaryotic type I DNA topoisomerase; 1.
DR   PROSITE; PS00396; TOPOISOMERASE_I_PROK; 1.
DR   PROSITE; PS50880; TOPRIM; 1.
PE   3: Inferred from homology;
KW   DNA-binding {ECO:0000256|ARBA:ARBA00023125, ECO:0000256|HAMAP-
KW   Rule:MF_00953};
KW   Isomerase {ECO:0000256|ARBA:ARBA00023235, ECO:0000256|HAMAP-Rule:MF_00953};
KW   Magnesium {ECO:0000256|HAMAP-Rule:MF_00953};
KW   Metal-binding {ECO:0000256|HAMAP-Rule:MF_00953};
KW   Reference proteome {ECO:0000313|Proteomes:UP000251213};
KW   Topoisomerase {ECO:0000256|ARBA:ARBA00023029, ECO:0000256|HAMAP-
KW   Rule:MF_00953}.
FT   DOMAIN          3..136
FT                   /note="Toprim"
FT                   /evidence="ECO:0000259|PROSITE:PS50880"
FT   REGION          187..192
FT                   /note="Interaction with DNA"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00953"
FT   ACT_SITE        311
FT                   /note="O-(5'-phospho-DNA)-tyrosine intermediate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00953"
FT   BINDING         9
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00953"
FT   BINDING         105
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00953"
FT   SITE            61
FT                   /note="Interaction with DNA"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00953"
FT   SITE            168
FT                   /note="Interaction with DNA"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00953"
FT   SITE            176
FT                   /note="Interaction with DNA"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00953"
FT   SITE            313
FT                   /note="Interaction with DNA"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00953"
SQ   SEQUENCE   732 AA;  84247 MW;  BE4EA1151607E300 CRC64;
     MGKTVVLAEK PSVGKDIAKV LHCHQQKNGY YEGDRYIVTW AFGHLVTLAD PERYKEAYKT
     WRLEDLPILP DRLKLVVIKK TSRQFQQVKT LMTRPDIKQI IIATDAGREG ELVARWIIEK
     TKVKKPIQRL WISSVTDKAI KEGFQRLRDG KQYENLYRSA VARAEADWIV GINATRALTC
     KHNAQLSCGR VQTPTLSMIA EREMEIRNFQ SKPFYGIEVT ADNLLKLTWQ NRKTNDGRIF
     SKEKCEQLLT KLKNQDGIIT EVKKTKKKRF APALYDLTEL QREANQRFGY SAKETLSILQ
     KLYEYHKVLT YPRTDSRYLS SDIVGTLKDR IEACRVGPYR TLASQAMKHL RPNKHFIDDR
     KVSDHHAIIP TEEPVILDKL SLKERKIYDL VVRRFLAVMY PPFEYEQTIV QVEIAGETFI
     ARGKVILAQG FKQVYEDYPE EEEKGEGIKE QILPKLERGS HLKIGSIVQT EGKTQPPEPF
     TEGTLIAAME NPVRFMKRER NDLIKTLGET GGLGTVATRA DIIEKLFATF LIEKKGKYIY
     ITSKGKQLLD LVPEELKSPA LTAEWEQKLA DIAKGKLNQD IFIKEMRKYA KDVVQEIKET
     TKAFKHDNLS TKKCPDCGKR LLEVKSKKGQ MLVCQDRTCG YRKGVARVTN ARCPECRKKL
     ELRGEGEGRI FVCGCGYREK YASFEKRKEK EKKGKVSKKE ITKYLKQQNQ LQEQGNPALK
     EALAKLFQKD GR
//
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